AnaSpec Releases 4 New Phosphospecific Anti-Tau Antibodies
San Jose, CA, November 23, 2008 --(PR.com)-- AnaSpec is excited to announce the release of 4 more new phosphospecific anti-Tau antibodies. This represents the industry’s largest collection of anti-Tau antibodies - 17 phosphospecific and 9 non-phosphospecific antibodies.
AnaSpec’s expertise in phosphopeptide synthesis combined with excellent affinity purification has resulted in the production of an anti-Tau to phosphoserine at position 235 (cat# 55315) clearly delineated from one at phosphoserine position 238 (cat# 55323). AnaSpec’s phosphospecific antibodies do not cross-react with each other.
Tau is a collection of microtubule-associated proteins that is involved in microtubule assembly and stabilization (1). In adult human brain, 6 isoforms, ranging between 352 and 441 amino acids in length, are produced as a result of alternative RNA splicing (2, 3). The expression of Tau isoforms is developmentally regulated, as only the smallest Tau polypeptide is expressed in the fetal brain. Hyperphosphorylated Tau is the major component of the paired helical filament of Alzheimer’s disease. Anti-phospho-Tau antibodies are used to identify specific amino acids that are phosphorylated in Tau from normal brains and Alzheimer’s disease brains. The Tau proteins, especially in developing brains and in Alzheimer brains, are phosphorylated in vivo at many different sites such as Thr181, Ser198, Ser199, Ser202, Thr205, Thr212, Ser214, Thr217, Thr231, Ser235, Ser262, Ser356, Ser396, Ser400, Ser404 and Ser413 (4, 5).
Rabbit anti-Phospho-Tau antibodies were raised against synthetic phosphopeptides. These antibodies were evaluated for specificity with ELISA and/or Western blot. By Western blot, an immunoreactive band around 52 kDa was observed in the mouse whole brain lysate. Species reactivity includes human, mouse and rat. Some antibodies have also shown reactivity with bovine, chicken and zebrafish.
Complementing one of the world’s most comprehensive collections of b-amyloid peptides, the availability of these anti-Tau antibodies demonstrates AnaSpec’s commitment to delivering integrated solutions for Alzheimer research.
About AnaSpec
AnaSpec is a leading provider of integrated proteomics solutions to the world’s largest biotech, pharmaceutical, and academic research institutions. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents, and combinatorial chemistry.
For more information visit www.anaspec.com
References:
1. Cleveland, DW. et al. J. Mol. Biol. 116, 207 (1977).
2. Goedert, M. et al. Neuron 3, 519 (1989).
3. Geodert, M. et al. EMBO J. 8, 393 (1989).
4. Billingsley, M. et al. Biochem J. 323, 577 (1997) .
5. Hanger, DP. et al. J. Neurochem. 71, 2465. (1998).
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AnaSpec’s expertise in phosphopeptide synthesis combined with excellent affinity purification has resulted in the production of an anti-Tau to phosphoserine at position 235 (cat# 55315) clearly delineated from one at phosphoserine position 238 (cat# 55323). AnaSpec’s phosphospecific antibodies do not cross-react with each other.
Tau is a collection of microtubule-associated proteins that is involved in microtubule assembly and stabilization (1). In adult human brain, 6 isoforms, ranging between 352 and 441 amino acids in length, are produced as a result of alternative RNA splicing (2, 3). The expression of Tau isoforms is developmentally regulated, as only the smallest Tau polypeptide is expressed in the fetal brain. Hyperphosphorylated Tau is the major component of the paired helical filament of Alzheimer’s disease. Anti-phospho-Tau antibodies are used to identify specific amino acids that are phosphorylated in Tau from normal brains and Alzheimer’s disease brains. The Tau proteins, especially in developing brains and in Alzheimer brains, are phosphorylated in vivo at many different sites such as Thr181, Ser198, Ser199, Ser202, Thr205, Thr212, Ser214, Thr217, Thr231, Ser235, Ser262, Ser356, Ser396, Ser400, Ser404 and Ser413 (4, 5).
Rabbit anti-Phospho-Tau antibodies were raised against synthetic phosphopeptides. These antibodies were evaluated for specificity with ELISA and/or Western blot. By Western blot, an immunoreactive band around 52 kDa was observed in the mouse whole brain lysate. Species reactivity includes human, mouse and rat. Some antibodies have also shown reactivity with bovine, chicken and zebrafish.
Complementing one of the world’s most comprehensive collections of b-amyloid peptides, the availability of these anti-Tau antibodies demonstrates AnaSpec’s commitment to delivering integrated solutions for Alzheimer research.
About AnaSpec
AnaSpec is a leading provider of integrated proteomics solutions to the world’s largest biotech, pharmaceutical, and academic research institutions. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents, and combinatorial chemistry.
For more information visit www.anaspec.com
References:
1. Cleveland, DW. et al. J. Mol. Biol. 116, 207 (1977).
2. Goedert, M. et al. Neuron 3, 519 (1989).
3. Geodert, M. et al. EMBO J. 8, 393 (1989).
4. Billingsley, M. et al. Biochem J. 323, 577 (1997) .
5. Hanger, DP. et al. J. Neurochem. 71, 2465. (1998).
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Contact
AnaSpec, Inc.
Ping Yang
408-452-5055
www.anaspec.com
Contact
Ping Yang
408-452-5055
www.anaspec.com
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